Product Details

Purity

Greater than 90% as determined by SDS-PAGE.

Target Names

HMOX1

Uniprot No.

P09601

Research Area

Cardiovascular

Alternative Names

32 kD; bK286B10; D8Wsu38e; heat shock protein 32 kD; heat shock protein 32kD; Heat shock protein; Heme oxygenase (decycling) 1; Heme oxygenase 1; Hemox; HMOX 1; Hmox; Hmox1; HMOX1_HUMAN; HO 1; HO; HO-1; HO1 ; Hsp32

Species

Homo sapiens (Human)

Source

E.coli

Expression Region

3-288aa

Target Protein Sequence

RPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVALEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHEVGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQLYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRASNKVQDSAPVETPRGKPPLNTRSQAPLLRWVLTLSFLVATVAVGLYAM
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Mol. Weight

36.6kDa

Protein Length

Partial

Tag Info

N-terminal 6xHis-tagged

Form

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

3-7 business days

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Description

The region for expressing recombinant Human HMOX1 contains amino acids 3-288. The theoretical molecular weight of the HMOX1 protein is 36.6 kDa. This HMOX1 protein is produced using e.coli expression system. The HMOX1 gene fragment has been modified by fusing the N-terminal 6xHis tag, providing convenience in detecting and purifying the recombinant HMOX1 protein during the following stages.

Human heme oxygenase 1 (HMOX1) is a crucial enzyme that plays a central role in heme catabolism. It catalyzes the degradation of heme into biliverdin, carbon monoxide (CO), and ferrous iron. Biliverdin is subsequently converted into bilirubin, an antioxidant with anti-inflammatory properties. HMOX1 is induced by various stimuli, including oxidative stress, inflammation, and environmental factors. Its expression is regulated by the transcription factor NRF2, which binds to the antioxidant response element (ARE) in the HMOX1 promoter. The enzymatic products generated by HMOX1 have protective effects against oxidative stress and inflammation. Research on HMOX1 is extensive, exploring its implications in diverse areas such as cellular stress response, inflammation, immune regulation, and its potential therapeutic applications in conditions associated with oxidative damage.

Target Background

Function

Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.

Gene References into Functions

Study found that plasma HO-1 levels were low in patients with peripheral artery disease, in contrast to high levels in patients with coronary artery disease. PMID: 30159103
HO-1 is over-expressed in sera of psoriasis patients and is correlated with psoriasis extent and severity. PMID: 30105448
Pregnant women who subsequently develop severe preeclampsia show higher expression of HO-1. PMID: 30363976
Our findings identify survivin as a target of HO-1 and a mediator of adipocyte-induced survival in the metastatic niche. PMID: 29311669
the role of HO-1 in nervous system pointing out different molecular mechanisms possibly responsible for HO-1 up-regulation in nervous system homeostasis and neurodegeneration. PMID: 30071692
HO-1 may serve as a prognostic marker and a new target to modulate chemotherapeutic effects in patients with small-intestinal adenocarcinomas PMID: 29537718
The T allele of heme oxygenase 1 gene SNP polymorphism (rs2071746) is a risk factor for esophageal varices development in cirrhotics. PMID: 29877949
Data show that the ferroptotic process induced by heme oxygenase-1 (HO-1). overexpression indicated that HO-1 is a key mediator of BAY 11-7085 (BAY)-induced ferroptosis that operates through cellular redox regulation and iron accumulation. PMID: 29274359
Heme oxygenase activity increases after exercise in healthy volunteers. PMID: 29343136
Results show that HO-1 is overexpressed in pancreatic cancer (PC) cells, induces cell proliferation and SHH signaling pathway activation as well as resistance to anticancer therapy. PMID: 29620188
the expression of hsa_circRNA0054633 has a protective effect against high glucoseinduced endothelial cell dysfunction by targeting ROBO1 and HO1. PMID: 29693114
the 14 kDa HO-1 is shown to promote cell proliferation and an increase in relative telomere lengths in vivo and in vitro. PMID: 29660345
HO-1 plays a key role in protecting tumor cells from apoptosis, in a process that involves Smad7 and HDAC4/5 in apoptosis of B-ALL cells PMID: 29886060
HO-1 might be a potential marker for prediction of ovarian cancer prognosis and a target for ovarian cancer treatment PMID: 28808929
HO-1 was an important cellular factor against Dengue virus replication. PMID: 27553177
our results demonstrate that Pc-induced expression of HO-1 is mediated by the PKCA-Nrf-2/HO-1 pathway, and inhibits UVB-induced apoptotic cell death in primary skin cells. PMID: 29470442
HO-1 regulates macrophage activation via the SIRT1-p53 signaling network and regulates hepatocellular death in liver ischemia-reperfusion injury. PMID: 28842295
In light of a pivotal role of NRF2 and BACH1 in response to oxidative stress and regulation of HO-1, we examined if smoke-induced HO-1 expression is modulated through the NRF2/BACH1 axis. We demonstrated that smoke causes significant nuclear translocation of NRF2, but only a slight decrease in nuclear BACH1. PMID: 29125538
downregulation of HO-1 gene expression in patients with inflammatory bowel disease. PMID: 28770550
This study demonstrated that HO-1 plays a vital role in the development of gastric cancer and may serve as a therapeutic target of this type of cancer PMID: 29048628
Overexpression of HO-1 inhibited the increase in nucleus pulposus cell apoptosis after IL-1beta treatment and simultaneously inhibited the expression of p-P65. PMID: 29617687
We also found a subset of prostate cancer patient-derived xenografts and prostate cancer patient samples with mild HO-1 and low Gal-1 expression levels. These results highlight a novel function of a human-used drug as a means of boosting the antitumor response PMID: 28512172
Our data suggest that HO-1 exerts its inhibitory effect on Th17 cell differentiation by directly associating and blocking STAT3 phosphorylation. We speculate that hemin may be a potential therapeutic candidate for the treatment of other types of immune and pulmonary inflammatory-related diseases. PMID: 28580587
recipient promoter region (GT)n genotype may contribute to cardiac allograft vasculopathy development PMID: 28186648
study implies that DJ-1 may protect endothelial progenitor cells against Ang II-induced dysfunction by activating the PPARgamma/HO-1. PMID: 28600848
These results revealed that hemin treatment increased HMOX1 expression and inhibited TGFbetainduced epithelial-mesenchymal transition in MCF7 cells. PMID: 28627599
There was no association between HMOX1 gene promoter polymorphism and manifestation of Fabry Disease. PMID: 28951772
Most published Newborn studies demonstrated no effect of HO-1 promoter polymorphisms on the Neonatal Hyperbilirubinemia. PMID: 28206992
Genetic mutations within MAPK1 (rs6928, rs9340, rs11913721), HIF-1 (rs1087314, rs2057482), and HO-1 (rs2071746) could alter susceptibility to perimenopausal coronary artery disease in Chinese population. PMID: 28444966
The overexpression of HO1 alleviated oxidative damage through inhibition of the PI3K/AKT signaling pathway and downregulation of the expression of cMyc. PMID: 28713890
Study shows that heme degradation by HO-1 is required for aggresome-like induced structures (ALIS) formation, and that the free iron released on heme degradation is necessary and sufficient to induce ALIS. PMID: 27821769
co-expression patterns of NGF and heme oxygenase-1 might be used as prognostic indicators for gastric carcinoma patients PMID: 28679437
These results suggest that HO-1 is involved in oxygen-glucose deprivation-evoked upregulation of apical junctional complex proteins, which is partly mediated by MMP9 pathway. PMID: 29425821
HMOX-1, an anti-oxidase, is a bona fide transcriptional target gene of HSF4 in HLECs (human lens epithelial cells). HSF4 directly binds to the HSE element in HMOX-1 promoter to mediate its mRNA transcription and protein accumulation. PMID: 29454088
The regulated HO-1 expression of Bone marrow stromal cells provides a new putative target for chronic myeloid leukemia therapy. PMID: 28445830
Dihydromyricetin (DMY) protects HUVECs from ox-LDL-induced oxidative injury by activating Akt and ERK1/2, which subsequently activates Nrf2/HO-1 signaling, thereby up-regulating antioxidant enzymes and anti-apoptotic proteins. PMID: 28612103
review of non-canonical functions of the HO isoforms: protein-protein interaction, intracellular compartmentalization, and extracellular secretion [review] PMID: 27626166
The interaction between ALAD rs1800435 and the HMOX1 rs2071746, HMOX1 rs2071747 was not associated with essential tremor. PMID: 28276576
Docosahexaenoic acid (DHA) activates Nrf2, possibly through modification of critical Keap1 cysteine 288 residue and PKCdelta-mediated phosphorylation of Nrf2, leading to upregulation of HO-1 and NQO1 expression. PMID: 28604588
These results suggest that RYR extract serves as alternative and complementary medicine in the treatment of these diseases, by inducing HO-1, thereby decreasing the vascular complications of diabetes PMID: 28555162
These results indicate that TNFRI-Fc and hHO-1 overexpression may apparently induce free iron in the liver and exert oxidative stress by enhancing reactive oxygen species production and block normal postneonatal liver metabolism. PMID: 28503569
Mice overexpressing human HO-1 specifically in astrocytes are protected from collagenase-induced intracerebral hemorrhage, as examined by striatal cell viability, neurological deficits and mortality. PMID: 28323022
HMOX1 negatively regulates MMP-9 expression in chronic lymphocytic leukemia cells in response to arsenic trioxide, through modulation of the p38 MAPK/AP-1 signaling pathway. PMID: 27829220
Review/Meta-analysis: both the HO-1(GT)n repeat length polymorphism and the T(-413)A SNP are associated with decreased risk of coronary heart disease. The (GT)n repeat length polymorphism was associated with coronary restenosis following PCI. PMID: 27825138
These data suggest that heme oxygenase-1 is induced during acute HIV-1 infection, likely mediating anti-inflammatory effects and driving expansion of heme oxygenase-1-specific CD8 regulatory T cells capable of suppressing HIV-1-specific immune responses in vitro. PMID: 28060008
Among myelodysplastic syndromes patients only, CD163 + macrophage density and HO1 and H-ferritin expression by CD163 + macrophages increased in tandem with marrow iron. High HO1 was significantly associated with shorter overall survival. PMID: 26758041
elevated HMOX1 expression is associated with stemness in Glioblastoma multiforme and can be modulated through TGFbeta. PMID: 27354342
Fetal GTn Repeat in the Heme Oxygenase 1 Promoter Is Associated With Severe and Early-Onset Preeclampsia. PMID: 29203625
CAL suppresses the expression of pro-inflammatory cytokines via p62/Nrf2-linked HO-1 induction in RASFs. PMID: 27678042
Findings indicate the importance of nuclear heme oxygenase-1 (HO-1) post-translational modification in the induction of cancer progression. PMID: 28846111

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Involvement in disease

Heme oxygenase 1 deficiency (HMOX1D)

Subcellular Location

Microsome. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side.

Protein Families

Heme oxygenase family

Tissue Specificity

Expressed at higher levels in renal cancer tissue than in normal tissue (at protein level).

Database Links

HGNC: 5013

OMIM: 141250

KEGG: hsa:3162

STRING: 9606.ENSP00000216117

UniGene: Hs.517581

Code	CSB-EP010583HU
Abbreviation	Recombinant Human HMOX1 protein, partial
MSDS	MSDS Datasheet
Size	$224
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Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Recombinant Human Heme oxygenase 1 (HMOX1), partial

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